Muscle protein oxidation and functionality: a global view of a once neglected phenomenon

Abstract

Muscle is a highly organized apparatus with a hierarchicmicrostructure that offers the protection of cellular components againstreactive oxygen species (ROS). However, fresh meat immediately postmortem andmeat undergoing processing become susceptible to oxidation due to physicaldisruption and the influx of molecular oxygen. Upon the activation byendogenous prooxidants, oxygen species are rapidly produced, and bothmyofibrillar and sarcoplasmic proteins become their primary targets. Direct ROSattack of amino acid sidechains and peptide backbone leads to proteinconformational changes, conversion to carbonyl and thiol derivatives, andsubsequent aggregation and polymerization. Interestingly, mild radical andnonradical oxidation enables orderly protein physicochemical changes, which explainswhy gels formed by ROS-modified myofibrillar protein has improved rheologicalproperties and binding potential in comminuted meat and meat emulsions. Theincorporation of phenolic and other multi-functional compounds promotes gelnetwork formation, fat emulsification, and water immobilization; however,extensive protein modification induced by high levels of ROS impairs proteinfunctionality. Now recognized to be a natural occurrence, once-neglectedprotein oxidation has drawn much interest and is being intensively studiedwithin the international community of meat science. This review describes thehistory and evolution of muscle protein oxidation, the mechanism andfunctionality impact hereof, and innovative oxidant/antioxidant strategies tocontrol and manipulate oxidation in the context of meat processing, storage,and quality. It is hoped that the review will stimulate in-depth discussion of scientificas well as industrial relevance and importance of protein oxidation and inspirerobust international collaboration in addressing this global challenge.